PURIFICATION AND CHARACTERIZATION OF GLUE LIKE SERICIN PROTEIN FROM A WILD SILKWORM Antheraea assamensis Helfer

Sericin is a hot water soluble glycoprotein and has been partially characterized in the domesticated silkworm Bombyx mori. Contrary to this very little information is available about the sericin of non mulberry silkworms. Sericin is generally a waste product during degumming. Recent advancement in silkworm research has revealed the use of sericin of B. mori as protein based biomaterial involving preparation of sericin 2D and 3D matrices, hydrogels and growth of fibroblast cells on sericin biofilms. The present study discusses the properties of sericin extracted from a wild silkworm Antheraea assamensis (Muga Silkworm) confined to the North Eastern Region of India and producing the golden hued muga silk. Molecular weight determination was done by SDSPAGE. Sericin was characterized using SEM, FT-IR, XRD, and DSC. SDSPAGE of sericin showed presence of both high and low molecular weight fractions. Surface morphology by SEM showed a rough surface along with aggregation of small particles of size around 12 μm. Structure determination by FT-IR and XRD revealed the presence of both αhelical and βsheet structures. Thermal properties were studied by DSC showing a degradation temperature around 363C. It is expected that this study will be helpful in exploiting sericin as potential biomaterial in biomedical and allied fields.